[Interaction investigation of trypsin inhibitor from sea anemone Radianthus macrodactylus with proteases]

Biomed Khim. 2006 Nov-Dec;52(6):595-600.
[Article in Russian]

Abstract

The interaction of inhibitor VJ (InhVJ), isolated from sea anemone R. macrodactylus, with different proteases was investigated. The following enzymes were tested: serine proteases (trypsin, alpha-chymotrypsin, plasmin, thrombin, kallikrein), cysteine protease (papain) and aspartic protease (pepsin). Inhibitor VJ interacted only with trypsin and 6-chymotrypsin. Kinetic and thermodynamics parameters of intermolecular complexes formation were determined: KD = 7,38 x 10(-8) M and 9,93 x 10(-7) M for pairs InhVJ/trypsin and InhVJ/alpha-chymotrypsin, respectively.

Publication types

  • Comparative Study
  • English Abstract
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Humans
  • Kinetics
  • Peptide Hydrolases / chemistry*
  • Peptide Hydrolases / metabolism
  • Protein Binding
  • Sea Anemones / chemistry*
  • Sea Anemones / metabolism
  • Trypsin Inhibitors / chemistry*
  • Trypsin Inhibitors / isolation & purification
  • Trypsin Inhibitors / metabolism

Substances

  • Trypsin Inhibitors
  • Peptide Hydrolases